penta N-benzoyl-apramycin | 1428669-42-4

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: penta N-benzoyl-apramycin
• 英文别名: N-[(1R,2S,3R,4R,5S)-4-[[(2R,3S,4R,4aR,6S,7R,8aS)-7-benzamido-2-[(2R,3R,4S,5S,6S)-5-benzamido-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-3-[benzoyl(methyl)amino]-4-hydroxy-2,3,4,4a,6,7,8,8a-octahydropyrano[3,2-b]pyran-6-yl]oxy]-5-benzamido-2,3-dihydroxycyclohexyl]benzamide
• CAS: 1428669-42-4
• 化学式: C₅₆H₆₁N₅O₁₆
• 分子量: 1060.12
• InChiKey: LATNTXDZWXHUCS-GQNDUYMZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.2
• 重原子数：
  77
• 可旋转键数：
  15
• 环数：
  9.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  304
• 氢给体数：
  10
• 氢受体数：
  16

反应信息

• 作为产物：
  描述：

  安普霉素 、 苯甲酰氯 在 sodium carbonate 作用下， 以 甲醇 、 水 为溶剂， 以14%的产率得到penta N-benzoyl-apramycin
  参考文献：
  名称：

  Selective Inhibition of Bacterial and Human Topoisomerases by N-Arylacyl O-Sulfonated Aminoglycoside Derivatives

  摘要：

  Numerous therapeutic applications have been proposed for molecules that bind heparin-binding proteins. Development of such compounds has primarily focused on optimizing the degree and orientation of anionic groups on a scaffold, but utility of these polyanions has been diminished by their typically large size and nonspecific interactions with many proteins. In this study, N-arylacyl O-sulfonated aminoglycosides were synthesized and evaluated for their ability to selectively inhibit structurally similar bacterial and human topoisomerases. It is demonstrated that the structure of the aminoglycoside and of the N-arylacyl moiety imparts selective inhibition of different topoisomerases and alters the mechanism. The results here outline a strategy that will be applicable to identifying small, structurally defined oligosaccharides that bind heparin-binding proteins with a high degree of selectivity.

  DOI：

  10.1021/ml3004507

文献信息

• Selective Inhibition of Bacterial and Human Topoisomerases by <i>N</i>-Arylacyl <i>O</i>-Sulfonated Aminoglycoside Derivatives
  作者：Amanda M. Fenner、Lisa M. Oppegard、Hiroshi Hiasa、Robert J. Kerns

  DOI：10.1021/ml3004507

  日期：2013.5.9

  Numerous therapeutic applications have been proposed for molecules that bind heparin-binding proteins. Development of such compounds has primarily focused on optimizing the degree and orientation of anionic groups on a scaffold, but utility of these polyanions has been diminished by their typically large size and nonspecific interactions with many proteins. In this study, N-arylacyl O-sulfonated aminoglycosides were synthesized and evaluated for their ability to selectively inhibit structurally similar bacterial and human topoisomerases. It is demonstrated that the structure of the aminoglycoside and of the N-arylacyl moiety imparts selective inhibition of different topoisomerases and alters the mechanism. The results here outline a strategy that will be applicable to identifying small, structurally defined oligosaccharides that bind heparin-binding proteins with a high degree of selectivity.